The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Neuronal α-Bungarotoxin Receptors Are α7 Subunit Homomers
Open accessAbstract
Nicotinic acetylcholine receptors in the nervous system are heterogeneous with distinct pharmacological and functional properties resulting from differences in post-translational processing and subunit composition. Because of nicotinic receptor diversity, receptor purification and biochemical characterization have been difficult, and the precise subunit composition of each receptor subtype is poorly characterized. Evidence is presented that α-bungarotoxin (Bgt)-binding nicotinic receptors found in pheochromocytoma 12 (PC12) cells are pentamers composed solely of α7 subunits. Metabolically labeled, affinity-purified Bgt receptors (BgtRs) consisted of a single 55 kDa band on SDS gels, which was recognized by anti-α7 antibodies on immunoblots. Isoelectric focusing separated the 55 kDa band into multiple spots, all recognized by anti-α7 antibodies and, therefore, each a differentially processed α7 subunit. Cell-surface BgtR subunits, cross-linked to each other and 125 I-Bgt, migrated on gels as a ladder of five bands with each band a multiple of an α7 subunit monomer. Similar characteristics of BgtRs from rat brain suggest that they, like PC12 BgtRs, are α7 pentamers containing differentially processed α7 subunits.
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Cites
Nicotine enhancement of fast excitatory synaptic transmission in CNS by presynaptic receptors
McGehee, D. S., Heath, M. J. S., Gelber, S., Devay, P., & Role, L. W. (1995) · Science · doi:10.1126/science.7569895 · Cited by 1,070
alpha-Bungarotoxin-sensitive hippocampal nicotinic receptor channel has a high calcium permeability
Castro, N. G., & Albuquerque, E. X. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)80213-4 · Cited by 273
Cited by
Nicotinic acetylcholine receptor α7 subunit is an essential regulator of inflammation
Wang, H., Yu, M., Ochani, M., Amella, C. A., Tanovic, M., Susarla, S., Li, J. H., Wang, H., Yang, H., Ulloa, L., et al. (2003) · Nature · doi:10.1038/nature01339 · Cited by 3,228
Mammalian nicotinic acetylcholine receptors: from structure to function
Albuquerque, E. X., Pereira, E. F. R., Alkondon, M., & Rogers, S. W. (2009) · Physiological Reviews · doi:10.1152/physrev.00015.2008 · Cited by 1,724
de Jonge, W. J., van der Zanden, E. P., The, F. O., Bijlsma, M. F., van Westerloo, D. J., Bennink, R. J., Berthoud, H.-R., Uematsu, S., Akira, S., van den Wijngaard, R. M., et al. (2005) · Nature Immunology · doi:10.1038/ni1229 · Cited by 1,074
Long-term potentiation of excitatory inputs to brain reward areas by nicotine
Mansvelder, H. D., & McGehee, D. S. (2000) · Neuron · doi:10.1016/s0896-6273(00)00042-8 · Cited by 720
Diversity of vertebrate nicotinic acetylcholine receptors
Millar, N. S., & Gotti, C. (2009) · Neuropharmacology · doi:10.1016/j.neuropharm.2008.07.041 · Cited by 441
Metadata
- Authors
- Drisdel, R. C., & Green, W. N.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2000-01-01
- Volume
- 20
- Issue
- 1
- Pages
- 133-139
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- OpenAlex
- W1785917080
- Cited by
- 215
- References
- 2
- FWCI
- 7.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
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